1-cys peroxiredoxin a biofunctional enzyme with glutathione peroxidase Oxidation of 6 in the Presence of GSH Increases its Phospholipase A2 Activity at Cytoplasmic pH Modeling the Catalytic Cycle of
Modeling the Catalytic Cycle of Glutathione Peroxidase by Nuclear Magnetic Resonance Spectroscopic Analysis of Selenocysteine Selenenic Acids Journal of the American Chemical Society Active site plasticity revealed in the asymmetric dimer of AnPrx6 the 1 Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120 Scientific Reports Peroxiredoxin 6 (human, recombinant) (aiPLA2, Acidic Calcium independent Phospholipase A2, 1 Cys Peroxiredoxin, Glutathione dependent Peroxiredoxin, LPCAT5, Non selenium Glutathione Peroxidase, NSGPx, PRDX6, Prx6) Cayman Chemical Human Peroxiredoxin 6 (hPrdx6): Structure, Biological Functions and Pathophysiological Importance IntechOpen Selenocysteine containing Glutathione peroxidase biosynthesis model Download Scientific Diagram
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